Rhodobacter sphaeroides haem protein

a novel cytochrome with nitric oxide dioxygenase activity

Bor-Ran Li, J L Ross Anderson, Christopher G Mowat, Caroline S Miles, Graeme A Reid, Stephen K Chapman

    Research output: Contribution to journalArticle

    Abstract

    Rhodobacter sphaeroides produces a novel cytochrome, designated as SHP (sphaeroides haem protein), that is unusual in having asparagine as a redox-labile haem ligand. The gene encoding SHP is contained within an operon that also encodes a DHC (dihaem cytochrome c) and a membrane-associated cytochrome b. DHC and SHP have been shown to have high affinity for each other at low ionic strength (K-d = 0.2 mu M), and DHC is able to reduce SHP very rapidly. The reduced form of the protein, SHp(2+) (reduced of ferrous SHP), has high affinity for both oxygen and nitric oxide (NO). it has been shown that the oxyferrous form, SHp(2+) -O-2 (oxygen-bound form of SHP), reacts rapidly with NO to produce nitrate, whereas SHp(2+)-NO (the No-bound form of SHP) will react with superoxide with the same product formed. it is therefore possible that SHP functions physiologically as a nitric oxide dioxygenase, protecting the organism against NO poisoning, and we propose a possible mechanism for this process.

    Original languageEnglish
    Pages (from-to)992-995
    Number of pages4
    JournalBiochemical Society Transactions
    Volume36
    Issue number5
    DOIs
    Publication statusPublished - Oct 2008
    Event3rd Intracellular Proteolysis Meeting - Canary Isl, Spain
    Duration: 5 Mar 20087 Mar 2008

    Fingerprint

    Rhodobacter sphaeroides
    Cytochromes
    Heme
    Proteins
    Nitric Oxide
    Cytochromes c
    Cytochromes a
    Oxygen
    nitric oxide dioxygenase
    Cytochromes b
    Asparagine
    Operon
    Superoxides
    Nitrates
    Osmolar Concentration
    Poisoning
    Oxidation-Reduction
    Ligands
    Membranes

    Keywords

    • Rhodobacter sphaeroides
    • MECHANISM
    • LIGAND-BINDING
    • c-type cytochrome
    • crystal structure
    • OXYGEN
    • NEUROGLOBIN
    • sphaeroides haem protein
    • nitric oxide dioxygenase
    • dihaem cytochrome c
    • FLAVOHEMOGLOBIN

    Cite this

    Li, B-R., Anderson, J. L. R., Mowat, C. G., Miles, C. S., Reid, G. A., & Chapman, S. K. (2008). Rhodobacter sphaeroides haem protein: a novel cytochrome with nitric oxide dioxygenase activity. Biochemical Society Transactions, 36(5), 992-995. https://doi.org/10.1042/BST0360992
    Li, Bor-Ran ; Anderson, J L Ross ; Mowat, Christopher G ; Miles, Caroline S ; Reid, Graeme A ; Chapman, Stephen K. / Rhodobacter sphaeroides haem protein : a novel cytochrome with nitric oxide dioxygenase activity. In: Biochemical Society Transactions. 2008 ; Vol. 36, No. 5. pp. 992-995.
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    Li, B-R, Anderson, JLR, Mowat, CG, Miles, CS, Reid, GA & Chapman, SK 2008, 'Rhodobacter sphaeroides haem protein: a novel cytochrome with nitric oxide dioxygenase activity', Biochemical Society Transactions, vol. 36, no. 5, pp. 992-995. https://doi.org/10.1042/BST0360992

    Rhodobacter sphaeroides haem protein : a novel cytochrome with nitric oxide dioxygenase activity. / Li, Bor-Ran; Anderson, J L Ross; Mowat, Christopher G; Miles, Caroline S; Reid, Graeme A; Chapman, Stephen K.

    In: Biochemical Society Transactions, Vol. 36, No. 5, 10.2008, p. 992-995.

    Research output: Contribution to journalArticle

    TY - JOUR

    T1 - Rhodobacter sphaeroides haem protein

    T2 - a novel cytochrome with nitric oxide dioxygenase activity

    AU - Li, Bor-Ran

    AU - Anderson, J L Ross

    AU - Mowat, Christopher G

    AU - Miles, Caroline S

    AU - Reid, Graeme A

    AU - Chapman, Stephen K

    N1 - M1 - Article

    PY - 2008/10

    Y1 - 2008/10

    N2 - Rhodobacter sphaeroides produces a novel cytochrome, designated as SHP (sphaeroides haem protein), that is unusual in having asparagine as a redox-labile haem ligand. The gene encoding SHP is contained within an operon that also encodes a DHC (dihaem cytochrome c) and a membrane-associated cytochrome b. DHC and SHP have been shown to have high affinity for each other at low ionic strength (K-d = 0.2 mu M), and DHC is able to reduce SHP very rapidly. The reduced form of the protein, SHp(2+) (reduced of ferrous SHP), has high affinity for both oxygen and nitric oxide (NO). it has been shown that the oxyferrous form, SHp(2+) -O-2 (oxygen-bound form of SHP), reacts rapidly with NO to produce nitrate, whereas SHp(2+)-NO (the No-bound form of SHP) will react with superoxide with the same product formed. it is therefore possible that SHP functions physiologically as a nitric oxide dioxygenase, protecting the organism against NO poisoning, and we propose a possible mechanism for this process.

    AB - Rhodobacter sphaeroides produces a novel cytochrome, designated as SHP (sphaeroides haem protein), that is unusual in having asparagine as a redox-labile haem ligand. The gene encoding SHP is contained within an operon that also encodes a DHC (dihaem cytochrome c) and a membrane-associated cytochrome b. DHC and SHP have been shown to have high affinity for each other at low ionic strength (K-d = 0.2 mu M), and DHC is able to reduce SHP very rapidly. The reduced form of the protein, SHp(2+) (reduced of ferrous SHP), has high affinity for both oxygen and nitric oxide (NO). it has been shown that the oxyferrous form, SHp(2+) -O-2 (oxygen-bound form of SHP), reacts rapidly with NO to produce nitrate, whereas SHp(2+)-NO (the No-bound form of SHP) will react with superoxide with the same product formed. it is therefore possible that SHP functions physiologically as a nitric oxide dioxygenase, protecting the organism against NO poisoning, and we propose a possible mechanism for this process.

    KW - Rhodobacter sphaeroides

    KW - MECHANISM

    KW - LIGAND-BINDING

    KW - c-type cytochrome

    KW - crystal structure

    KW - OXYGEN

    KW - NEUROGLOBIN

    KW - sphaeroides haem protein

    KW - nitric oxide dioxygenase

    KW - dihaem cytochrome c

    KW - FLAVOHEMOGLOBIN

    U2 - 10.1042/BST0360992

    DO - 10.1042/BST0360992

    M3 - Article

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    SP - 992

    EP - 995

    JO - Biochemical Society Transactions

    JF - Biochemical Society Transactions

    SN - 0300-5127

    IS - 5

    ER -